In SDS gels of purified, highly active ATP-synthase from chloroplasts, CF0F1 a protein band was detected at an apparent molecular weight of 100 kDa. This protein was isolated on a preparative SDS gel. The 100 kDa protein can be dissociated at increased temperature or increased incubation time into an 8 kDa protein, which is identical with the subunit III of CF0 (DCCD- binding protein or proteolipid). This implies that the 100 kDa band is a stable supramolccular complex containing at least 12 copies of subunit III. Electron micrographs reveal a diameter of 6.3 nm and a membrane spanning length of 6.1 nm. We assume that this supramolecular complex represents a stable native substructure of CF0F1.
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